All organisms respond to heat by inducing the synthesis of a group of proteins called the
heat-shock proteins or hsps. The response is the most highly conserved genetic system …

In the cell, as in vitro, the final conformation of a protein is determined by its amino-acid
sequence. But whereas some isolated proteins can be denatured and refolded in vitro in the …

The N-ethylmaleimide-sensitive fusion protein (NSF) and the soluble NSF attachment
proteins (SNAPs) appear to be essential components of the intracellular membrane fusion …

HSPA8/HSC70 protein is a fascinating chaperone protein. It represents a constitutively
expressed, cognate protein of the HSP70 family, which is central in many cellular processes …

A 73-kilodalton (kD) intracellular protein was found to bind to peptide regions that target
intracellular proteins for lysosomal degradation in response to serum withdrawal. This …

Lysosomes take up and degrade intracellular proteins in cultured cells in response to serum
deprivation, and in tissues of organisms in response to starvation. One mechanism by which …

The three-dimensional structure of the amino-terminal 44K ATPase fragment of the 70K
bovine heat-shock cognate protein has been solved to a resolution of 2.2 Å. The ATPase …

The 70-kilodalton family of heat shock proteins (Hsp 70) has been implicated in
posttranslational protein assembly and translocation. Binding of cytosolic forms of Hsp 70 …

It is a general feature of molecular chaperones that they are highly conserved throughout
evolution. Prokaryotic and eukaryotic Hsp70 proteins, for example, are over 50% identical at …

The products of the Escherichia coli dnaK, dnaJ, and grpE heat shock genes have been
previously shown to be essential for bacteriophage lambda DNA replication at all …